MALDI-target integrated platform for affinity-captured protein digestion

To address immunocapture of proteins in large cohorts of clinical samples high throughput sample processing is required. Here a method using the proteomic sample platform, ISET (integrated selective enrichment target) that integrates highly specific immunoaffinity capture of protein biomarker, diges...

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Main Authors: Ahmad Tajudin, Asilah, Adler, Belinda, Ekstrom, Simon, Marko-Varga, Gyorgy, Malm, Johan, Lilja, Hans, Laurell, Thomas
Format: Article
Published: Elsevier 2014
Online Access:http://psasir.upm.edu.my/id/eprint/34429/
http://www.sciencedirect.com/science/article/pii/S0003267013011689
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spelling my.upm.eprints.344292015-12-15T03:02:55Z http://psasir.upm.edu.my/id/eprint/34429/ MALDI-target integrated platform for affinity-captured protein digestion Ahmad Tajudin, Asilah Adler, Belinda Ekstrom, Simon Marko-Varga, Gyorgy Malm, Johan Lilja, Hans Laurell, Thomas To address immunocapture of proteins in large cohorts of clinical samples high throughput sample processing is required. Here a method using the proteomic sample platform, ISET (integrated selective enrichment target) that integrates highly specific immunoaffinity capture of protein biomarker, digestion and sample cleanup with a direct interface to mass spectrometry is presented. The robustness of the on-ISET protein digestion protocol was validated by MALDI MS analysis of model proteins, ranging from 40 fmol to 1 pmol per nanovial. On-ISET digestion and MALDI MS/MS analysis of immunoaffinity captured disease-associated biomarker PSA (prostate specific antigen) from human seminal plasma are presented. Elsevier 2014-01-07 Article PeerReviewed Ahmad Tajudin, Asilah and Adler, Belinda and Ekstrom, Simon and Marko-Varga, Gyorgy and Malm, Johan and Lilja, Hans and Laurell, Thomas (2014) MALDI-target integrated platform for affinity-captured protein digestion. Analytica Chimica Acta, 807. pp. 1-8. ISSN 0003-2670; ESSN: 1873-4324 http://www.sciencedirect.com/science/article/pii/S0003267013011689 10.1016/j.aca.2013.08.051
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
description To address immunocapture of proteins in large cohorts of clinical samples high throughput sample processing is required. Here a method using the proteomic sample platform, ISET (integrated selective enrichment target) that integrates highly specific immunoaffinity capture of protein biomarker, digestion and sample cleanup with a direct interface to mass spectrometry is presented. The robustness of the on-ISET protein digestion protocol was validated by MALDI MS analysis of model proteins, ranging from 40 fmol to 1 pmol per nanovial. On-ISET digestion and MALDI MS/MS analysis of immunoaffinity captured disease-associated biomarker PSA (prostate specific antigen) from human seminal plasma are presented.
format Article
author Ahmad Tajudin, Asilah
Adler, Belinda
Ekstrom, Simon
Marko-Varga, Gyorgy
Malm, Johan
Lilja, Hans
Laurell, Thomas
spellingShingle Ahmad Tajudin, Asilah
Adler, Belinda
Ekstrom, Simon
Marko-Varga, Gyorgy
Malm, Johan
Lilja, Hans
Laurell, Thomas
MALDI-target integrated platform for affinity-captured protein digestion
author_facet Ahmad Tajudin, Asilah
Adler, Belinda
Ekstrom, Simon
Marko-Varga, Gyorgy
Malm, Johan
Lilja, Hans
Laurell, Thomas
author_sort Ahmad Tajudin, Asilah
title MALDI-target integrated platform for affinity-captured protein digestion
title_short MALDI-target integrated platform for affinity-captured protein digestion
title_full MALDI-target integrated platform for affinity-captured protein digestion
title_fullStr MALDI-target integrated platform for affinity-captured protein digestion
title_full_unstemmed MALDI-target integrated platform for affinity-captured protein digestion
title_sort maldi-target integrated platform for affinity-captured protein digestion
publisher Elsevier
publishDate 2014
url http://psasir.upm.edu.my/id/eprint/34429/
http://www.sciencedirect.com/science/article/pii/S0003267013011689
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